cAMP-induced phosphorylation of 26S proteasomes on Rpn6/PSMD11 enhances their activity and the degradation of misfolded proteins.

@article{Lokireddy2015cAMPinducedPO,
  title={cAMP-induced phosphorylation of 26S proteasomes on Rpn6/PSMD11 enhances their activity and the degradation of misfolded proteins.},
  author={Sudarsanareddy Lokireddy and Nikolay Vadimovich Kukushkin and Alfred L Goldberg},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2015},
  volume={112 52},
  pages={E7176-85}
}
Although rates of protein degradation by the ubiquitin-proteasome pathway (UPS) are determined by their rates of ubiquitination, we show here that the proteasome's capacity to degrade ubiquitinated proteins is also tightly regulated. We studied the effects of cAMP-dependent protein kinase (PKA) on proteolysis by the UPS in several mammalian cell lines. Various agents that raise intracellular cAMP and activate PKA (activators of adenylate cyclase or inhibitors of phosphodiesterase 4) promoted… CONTINUE READING
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